alanyl-tRNA synthetase (Protein | Antibody | cDNA Clone | ELISA Kit)

All alanyl-tRNA synthetase reagents are produced in house and quality controlled, including 2 alanyl-tRNA synthetase Antibody, 16 alanyl-tRNA synthetase Gene, 2 alanyl-tRNA synthetase IP Kit, 2 alanyl-tRNA synthetase Lysate, 2 alanyl-tRNA synthetase Protein, 1 alanyl-tRNA synthetase qPCR. All alanyl-tRNA synthetase reagents are ready to use.

alanyl-tRNA synthetase Protein (2)

alanyl-tRNA synthetase Antibody (2)

alanyl-tRNA synthetase cDNA Clone (16)

alanyl-tRNA synthetase qPCR Primer (1)

alanyl-tRNA synthetase Lysate (2)

alanyl-tRNA synthetase Background

Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.

alanyl-tRNA synthetase References

  • Wakasugi K, et al. (1999) Two Distinct Cytokines Released from a Human Aminoacyl-tRNA Synthetase. Science. 284 (5411): 147-51.
  • Sokabe M, et al. (2009) The structure of alanyl-tRNA synthetase with editing domain. Proc Natl Acad Sci . 106 (27): 11028-33.
  • Skupinska M, et al. (2009) AARS--the etiological factor and the attractive target of many disorders. Postepy Biochem. 55 (4): 373-84.